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Database: UniProt
Entry: A0A0F5K5B6_9BURK
LinkDB: A0A0F5K5B6_9BURK
Original site: A0A0F5K5B6_9BURK 
ID   A0A0F5K5B6_9BURK        Unreviewed;       416 AA.
AC   A0A0F5K5B6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=(2Fe-2S)-binding protein {ECO:0000313|EMBL:KKB65044.1};
GN   ORFNames=WM40_02050 {ECO:0000313|EMBL:KKB65044.1};
OS   Robbsia andropogonis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Robbsia.
OX   NCBI_TaxID=28092 {ECO:0000313|EMBL:KKB65044.1, ECO:0000313|Proteomes:UP000033618};
RN   [1] {ECO:0000313|EMBL:KKB65044.1, ECO:0000313|Proteomes:UP000033618}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP2807 {ECO:0000313|EMBL:KKB65044.1,
RC   ECO:0000313|Proteomes:UP000033618};
RA   Lopes-Santos L., Castro D.B., Ottoboni L.M., Park D., Weirc B.S.,
RA   Destefano S.A.;
RT   "Draft Genome Sequence of Burkholderia andropogonis type strain ICMP2807,
RT   isolated from Sorghum bicolor.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKB65044.1}.
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DR   EMBL; LAQU01000002; KKB65044.1; -; Genomic_DNA.
DR   RefSeq; WP_024905896.1; NZ_JAIFTJ010000004.1.
DR   AlphaFoldDB; A0A0F5K5B6; -.
DR   STRING; 28092.WM40_02050; -.
DR   PATRIC; fig|28092.6.peg.478; -.
DR   OrthoDB; 9790995at2; -.
DR   Proteomes; UP000033618; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd08885; RHO_alpha_C_1; 1.
DR   CDD; cd03469; Rieske_RO_Alpha_N; 1.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR   InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR   InterPro; IPR001663; Rng_hydr_dOase-A.
DR   PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43756:SF5; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF00848; Ring_hydroxyl_A; 1.
DR   PRINTS; PR00090; RNGDIOXGNASE.
DR   SUPFAM; SSF55961; Bet v1-like; 1.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   PROSITE; PS51296; RIESKE; 1.
DR   PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033618}.
FT   DOMAIN          49..156
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
SQ   SEQUENCE   416 AA;  46366 MW;  1C5C3A11063937B1 CRC64;
     MPQAFDDAFF AGLETSTLPV GQAETLPPQC YTDPAFYEFE KEAVFNHEWL CVGRTDWIAK
     PGDFFTTSIV NEPLLIARNA RNEIKAMSAV CQHRAMLVAE GNGNTRAFLC PYHHWAYSLD
     GELIAAPAMD ATEGFDKKAF CLPTLLVETW QGFIFVNFDK EAAPLAPRLT ALDPVLANFE
     LDRAEGPRPS DAAHFPWNWK VMFENNNDGY HANRLHHGPL HDFVPSALAS FPDSLPEDTA
     GYYRFNGTIH ADAAFNPTQK ALFPIFPKLT DEERNRMLFA NVPPTLSLVV TVDSVIYMIL
     RADAAGTHHM DQGVLYAPGA MQDPLFQKRV ELSFSAVSDI VAQDLHVDEL VQKGLQSRFA
     IRGRYSWQER AQQELNAWLV PRYQAARQRI GKAAAARTTL EGAHARLAAI DVVTAS
//
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